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The complex interface between the helical bundle and the Rpn12 helix would in principle allow Rpn12 to sense and transmit signals through multiple lid subunits.
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Proteasome lid subunits are essential proteins for budding yeast viability; knocking-down any lid subunit (other than Rpn15/Sem1) in this organism results in lethality [ 5].
Glycerol gradient fractionation confirmed base-CP proteasome species lacking lid subunits in this mutant.
Without Rpn8, no complexes of Rpn11 with other lid subunits were detected.
No enzymatic information has been documented for lid subunits other than Rpn11.
In absence of Rpn5, this Rpn8 Rpn11 dimer was unable to recruit other lid subunits.
Likewise, MS/MS did not pick up peptides derived from lid subunits in these samples (3).
The Rpn11 subunit initiates assembly of a five-subunit lid module competent to integrate into pre-assembled base-20S core particle (CP), with subsequent recruitment of remaining lid subunits.
Initially thought to bridge the base and the lid because its absence destabilizes their interaction (Glickman et al. 1998), the ubiquitin receptor PSMD4/Rpn10 subunit was later shown to only bind to lid subunits (Tomko and Hochstrasser 2013).
Representative lid subunits, Rpn5, 8, 11 and 12, were also enriched in fractions containing proteasome holoenzymes, but trace amounts were found in lower Mr fractions, suggesting that a portion of lid subunits does not associate with 26S holoenzymes.
Base-CP, without any detectable lid subunits, typical of proteasomes purified in absence of Rpn10 [ 16], was also observed.
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